Drosophila CTP synthase regulates collective cell migration by controlling the polarized endocytic cycle

Author:

Wang Pei-Yu12ORCID,Chakraborty Archan13ORCID,Ma Hsin-Ju1,Wu Jhen-Wei4,Jang Anna C.-C.4,Lin Wei-Cheng15ORCID,Pi Hai-Wei67ORCID,Yeh Chau-Ting78,Cheng Mei-Ling67910,Yu Jau-Song1578ORCID,Pai Li-Mei1578ORCID

Affiliation:

1. College of Medicine, Chang Gung University 1 Department of Biochemistry and Molecular Biology , , Taoyuan 33302 , Taiwan

2. Research Center for Emerging Viral Infections, College of Medicine, Chang Gung University 2 , Taoyuan 33302 , Taiwan

3. Duke University 3 Pharmacology and Cancer Biology , , Durham, NC 27705 , USA

4. National Cheng Kung University 4 Department of Biotechnology and Bioindustry Sciences , , Tainan City 701 , Taiwan

5. Molecular Medicine Research Center, Chang Gung University 5 , Taoyuan 33302 , Taiwan

6. Department of Biomedical Sciences, College of Medicine, Chang Gung University 6 , Taoyuan 33302 , Taiwan

7. Graduate Institute of Biomedical Sciences, College of Medicine, Chang Gung University 7 , Taoyuan 33302 , Taiwan

8. Liver Research Center, Chang Gung Memorial Hospital 8 , Linkou 333423 , Taiwan

9. Healthy Aging Research Center, Chang Gung University 9 , Taoyuan 33302 , Taiwan

10. Chang Gung Memorial Hospital 10 Clinical Metabolomics Core Laboratory , , Linkou 333423 , Taiwan

Abstract

ABSTRACT Phosphatidylinositol (PI) 4,5-bisphosphate (PIP2) is involved in many biological functions. However, the mechanisms of PIP2 in collective cell migration remain elusive. This study highlights the regulatory role of cytidine triphosphate synthase (CTPsyn) in collective border cell migration through regulating the asymmetrical distribution of PIP2. We demonstrated that border cell clusters containing mutant CTPsyn cells suppressed migration. CTPsyn was co-enriched with Actin at the leading edge of the Drosophila border cell cluster where PIP2 was enriched, and this enrichment depended on the CTPsyn activity. Genetic interactions of border cell migration were found between CTPsyn mutant and genes in PI biosynthesis. The CTPsyn reduction resulted in loss of the asymmetric activity of endocytosis recycling. Also, genetic interactions were revealed between components of the exocyst complex and CTPsyn mutant, indicating that CTPsyn activity regulates the PIP2-related asymmetrical exocytosis activity. Furthermore, CTPsyn activity is essential for RTK-polarized distribution in the border cell cluster. We propose a model in which CTPsyn activity is required for the asymmetrical generation of PIP2 to enrich RTK signaling through endocytic recycling in collective cell migration.

Funder

Ministry of Science and Technology, Taiwan

Chang Gung Memorial Hospital

Publisher

The Company of Biologists

Subject

Developmental Biology,Molecular Biology

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